Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q46669 (CDTB_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytolethal distending toxin subunit B

Short name=CDT B
Alternative name(s):
Deoxyribonuclease CdtB
EC=3.1.-.-
Gene names
Name:cdtB
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Part of the tripartite complex that is required for the CDT activity. CdtB exhibits a DNA-nicking endonuclease activity, and very probably causes DNA damage in intoxicated cells. This damage induces G2/M cell cycle arrest, chromatin fragmentation, cell distention and nucleus enlargement. Ref.2

Subunit structure

Heterotrimer of 3 subunits, CdtA, CdtB and CdtC.

Subcellular location

Secreted. Note: Localized to the nucleus of the infected cells. Ref.4

Miscellaneous

The operon of the strain O128:H- / 9142-88 / EPEC is referred to as cdt type II (CDT-II).

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionEndonuclease
Hydrolase
Nuclease
Toxin
   Technical term3D-structure
Gene Ontology (GO)
   Biological processpathogenesis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionendonuclease activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 269251Cytolethal distending toxin subunit B
PRO_0000013373

Regions

Motif195 – 21016Nuclear localization signal Ref.4

Experimental info

Mutagenesis1541H → A: When the mutant protein is introduced in HeLa cells, it does not result in cell cycle arrest. Devoid of DNA-nicking/DNase activity. Ref.2 Ref.3
Mutagenesis2291D → A: Loss of DNase activity, no cellular distension, no G2/M cell cycle arrest. Ref.3
Mutagenesis2601D → R: Loss of DNase activity, no cellular distension, no G2/M cell cycle arrest. Ref.3
Mutagenesis2611H → A: Loss of DNase activity, no cellular distension, no G2/M cell cycle arrest. Ref.3

Secondary structure

................................................ 269
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q46669 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 958B09BD6C73EBB5

FASTA26929,529
        10         20         30         40         50         60 
MKKYIISLIV FLSFYAQADL TDFRVATWNL QGASATTESK WNINVRQLIS GENAVDILAV 

        70         80         90        100        110        120 
QEAGSPPSTA VDTGTLIPSP GIPVRELIWN LSTNSRPQQV YIYFSAVDAL GGRVNLALVS 

       130        140        150        160        170        180 
NRRADEVFVL SPVRQGGRPL LGIRIGNDAF FTAHAIAMRN NDAPALVEEV YNFFRDSRDP 

       190        200        210        220        230        240 
VHQALNWMIL GDFNREPADL EMNLTVPVRR ASEIISPAAA TQTSQRTLDY AVAGNSVAFR 

       250        260 
PSPLQAGIVY GARRTQISSD HFPVGVSRR 

« Hide

References

[1]"Cloning, sequencing, and expression of the Escherichia coli cytolethal distending toxin genes."
Pickett C.L., Cottle D.L., Pesci E.C., Bikah G.
Infect. Immun. 62:1046-1051(1994) [PubMed: 8112838] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: O128:H- / 9142-88 / EPEC.
[2]"Escherichia coli CdtB mediates cytolethal distending toxin cell cycle arrest."
Elwell C.A., Chao K., Patel K., Dreyfus L.A.
Infect. Immun. 69:3418-3422(2001) [PubMed: 11292766] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF HIS-154.
[3]"DNase I homologous residues in CdtB are critical for cytolethal distending toxin-mediated cell cycle arrest."
Elwell C.A., Dreyfus L.A.
Mol. Microbiol. 37:952-963(2000) [PubMed: 10972814] [Abstract]
Cited for: MUTAGENESIS OF HIS-154; ASP-229; ASP-260 AND HIS-261.
[4]"Nuclear localization of the Escherichia coli cytolethal distending toxin CdtB subunit."
McSweeney L.A., Dreyfus L.A.
Cell. Microbiol. 6:447-458(2004) [PubMed: 15056215] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION OF THE NUCLEAR LOCALIZATION SIGNAL.
[5]"Differences in crystal and solution structures of the cytolethal distending toxin B subunit: Relevance to nuclear translocation and functional activation."
Hontz J.S., Villar-Lecumberri M.T., Potter B.M., Yoder M.D., Dreyfus L.A., Laity J.H.
J. Biol. Chem. 281:25365-25372(2006) [PubMed: 16809347] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 19-269.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U04208 Unassigned DNA. Translation: AAA18786.1.
PIRI69095.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F1NX-ray1.73A19-269[»]
ProteinModelPortalQ46669.
SMRQ46669. Positions 19-268.
ModBaseSearch...

Protein family/group databases

TCDB1.C.98.1.1. cytolethal distending toxin (CDT) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR003539. CD_toxinB.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
PIRSFPIRSF018539. CDT_B. 1 hit.
PRINTSPR01388. CDTOXINB.
SUPFAMSSF56219. Exo_endo_phos. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCDTB_ECOLX
AccessionPrimary (citable) accession number: Q46669
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: November 1, 1996
Last modified: May 31, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references